Transcription Factor
Accessions: | 1l1m_A (3D-footprint 20231221), 1l1m_B (3D-footprint 20231221), 1osl_A (3D-footprint 20231221), 1osl_B (3D-footprint 20231221), 2kei_A (3D-footprint 20231221), 2kei_B (3D-footprint 20231221), 2kej_A (3D-footprint 20231221), 2kej_B (3D-footprint 20231221), 2kek_A (3D-footprint 20231221), 2kek_B (3D-footprint 20231221) |
Names: | LACI_ECOLI, Lactose operon repressor |
Organisms: | Escherichia coli, strain K12 |
Libraries: | 3D-footprint 20231221 1 1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed] |
Uniprot: | P03023 |
Length: | 62 |
Pfam Domains: | 5-50 Bacterial regulatory proteins, lacI family |
Sequence: (in bold interface residues) | 1 MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRCAQQLAGKQ 60 61 SL |
Interface Residues: | 6, 7, 16, 17, 18, 19, 21, 22, 28, 29, 30, 53, 56, 57 |
3D-footprint Homologues: | 7ce1_D, 1efa_B, 3oqm_C, 1l1m_B, 5ui5_I, 1zvv_A, 1jft_A, 4i2o_B |
Binding Motifs: | 1l1m_AB TTGTTATCCGCTCACAA 1l1m_B TTGTTATCCG 1osl_AB ATnAGATATCTTAT 1osl_B atwagata 2kei_AB TGTTATCCGCTCACAA 2kei_B TGTTATACG 2kej_A CGCTCACAtt 2kej_AB TGTTaCTCGCTCACA 2kek_AB CnntGCGCTCAC 2kek_B TnGCnnTGCG |
Binding Sites: | 1l1m_C / 2kei_C 1l1m_D / 2kei_D 1osl_C / 1osl_D 2kej_C 2kej_D 2kek_C 2kek_D |
Publications: | Kalodimos C.G, Bonvin A.M, Salinas R.K, Wechselberger R, Boelens R, Kaptein R. Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain. The EMBO journal 21:2866-76 (2002). [Pubmed] Kalodimos C.G, Biris N, Bonvin A.M, Levandoski M.M, Guennuegues M, Boelens R, Kaptein R. Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes. Science (New York, N.Y.) 305:386-9 (2004). [Pubmed] Romanuka J, Folkers G.E, Biris N, Tishchenko E, Wienk H, Bonvin A.M, Kaptein R, Boelens R. Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes. Journal of molecular biology 390:478-89 (2009). [Pubmed] |
Related annotations: | PaperBLAST |
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